Q09013 (DMPK_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Myotonin-protein kinase
Short name=MT-PK
EC=2.7.11.1

Alternative name(s):
DM-kinase
Short name=DMK
DM1 protein kinase
DMPK
Myotonic dystrophy protein kinase

Gene names

Name:	DMPK
Synonyms:	DM1PK, MDPK

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	629 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Non-receptor serine/threonine protein kinase which is necessary for the maintenance of skeletal muscle structure and function. May play a role in myocyte differentiation and survival by regulating the integrity of the nuclear envelope and the expression of muscle-specific genes. May also phosphorylate PPP1R12A and inhibit the myosin phosphatase activity to regulate myosin phosphorylation. Also critical to the modulation of cardiac contractility and to the maintenance of proper cardiac conduction activity probably through the regulation of cellular calcium homeostasis. Phosphorylates PLN, a regulator of calcium pumps and may regulate sarcoplasmic reticulum calcium uptake in myocytes. May also phosphorylate FXYD1/PLM which is able to induce chloride currents. May also play a role in synaptic plasticity. Ref.12 Ref.15 Ref.16 Ref.18 Ref.21 Ref.22
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Cofactor	Magnesium.
Enzyme regulation	Coiled-coil-mediated oligomerization enhances the catalytic activity. Proteolytic processing of the C-terminus may release the protein from membranes and constitute a mean to regulate the enzyme. May be regulated by HSPB2, RAC1, RAF1 and G-protein second messengers. Ref.11 Ref.12 Ref.13 Ref.17
Subunit structure	Homodimer; homodimerization stimulates the kinase activity. Interacts with HSPB2; may enhance DMPK kinase activity. Interacts with PLN; phosphorylates PLN. May interact with RAC1; may regulate DMPK kinase activity. Interacts with LMNA; may regulate nuclear envelope stability. Ref.11 Ref.12 Ref.13 Ref.17 Ref.18 Ref.22 Ref.24 Ref.25
Subcellular location	Endoplasmic reticulum membrane; Single-pass type IV membrane protein; Cytoplasmic side By similarity. Nucleus outer membrane; Single-pass type IV membrane protein; Cytoplasmic side Probable. Mitochondrion outer membrane; Single-pass type IV membrane protein Probable. Sarcoplasmic reticulum membrane By similarity. Cell membrane By similarity. Cytoplasm › cytosol By similarity. Note: Localizes to sarcoplasmic reticulum membranes of cardiomyocytes By similarity. Ref.12 Ref.19 Ref.22 Isoform 1: Mitochondrion membrane Ref.12 Ref.19 Ref.22. Isoform 3: Mitochondrion membrane Ref.12 Ref.19 Ref.22.
Tissue specificity	Most isoforms are expressed in many tissues including heart, skeletal muscle, liver and brain, except for isoform 2 which is only found in the heart and skeletal muscle, and isoform 14 which is only found in the brain, with high levels in the striatum, cerebellar cortex and pons. Ref.9
Domain	The coiled coil domain is required for homodimerization and regulates the enzymatic activity. Ref.23 Ref.24
Post-translational modification	Phosphorylated. Autophosphorylates. Phosphorylation by RAF1 may result in activation of DMPK. Ref.13 Proteolytic processing of the C-terminus may remove the transmembrane domain and release the kinase from membranes stimulating its activity.
Involvement in disease	Dystrophia myotonica 1 (DM1) [MIM:160900]: A muscular disorder characterized by myotonia, muscle wasting in the distal extremities, cataract, hypogonadism, defective endocrine functions, male baldness and cardiac arrhythmias. Note: The disease is caused by mutations affecting the gene represented in this entry. The causative mutation is a CTG expansion in the 3'-UTR of the DMPK gene. A length exceeding 50 CTG repeats is pathogenic, while normal individuals have 5 to 37 repeats. Intermediate alleles with 35-49 triplets are not disease-causing but show instability in intergenerational transmissions. Disease severity varies with the number of repeats: mildly affected persons have 50 to 150 repeats, patients with classic DM have 100 to 1,000 repeats, and those with congenital onset can have more than 2,000 repeats. Ref.1 Ref.8 Ref.10 Ref.20
Sequence similarities	Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. DMPK subfamily. Contains 1 AGC-kinase C-terminal domain. Contains 1 protein kinase domain.
Sequence caution	The sequence AAA64884.1 differs from that shown. Reason: Frameshift at positions 56, 555 and 568. The sequence AAA87583.1 differs from that shown. Reason: Probable cloning artifact.

Ontologies

Keywords
Cellular component	Cell membrane Cytoplasm Endoplasmic reticulum Membrane Mitochondrion Mitochondrion outer membrane Nucleus Sarcoplasmic reticulum
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Cataract
Domain	Coiled coil Transmembrane Transmembrane helix
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cellular calcium ion homeostasis Inferred from sequence or structural similarity. Source: UniProtKB muscle cell apoptotic process Inferred from direct assay PubMed 18729234. Source: UniProtKB nuclear envelope organization Inferred from mutant phenotype Ref.22. Source: UniProtKB regulation of excitatory postsynaptic membrane potential involved in skeletal muscle contraction Inferred from electronic annotation. Source: Compara regulation of heart contraction Inferred from direct assay Ref.18. Source: UniProtKB regulation of myotube differentiation Inferred from sequence or structural similarity. Source: UniProtKB regulation of skeletal muscle contraction by calcium ion signaling Inferred from electronic annotation. Source: Compara regulation of sodium ion transport Inferred from electronic annotation. Source: Compara regulation of synapse structural plasticity Inferred from electronic annotation. Source: Compara
Cellular_component	cytosol Inferred from sequence or structural similarity. Source: UniProtKB integral to mitochondrial outer membrane Inferred from direct assay Ref.19. Source: UniProtKB nuclear membrane Inferred from sequence or structural similarity. Source: UniProtKB nuclear outer membrane Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from sequence or structural similarity. Source: UniProtKB sarcoplasmic reticulum membrane Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	ATP binding Inferred from direct assay Ref.12. Source: UniProtKB metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW myosin phosphatase regulator activity Inferred from direct assay Ref.16. Source: UniProtKB protein serine/threonine kinase activity Inferred from direct assay Ref.12Ref.16. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
PLN	P26678	4	EBI-692774,EBI-692836

Alternative products

This entry describes 12 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q09013-9)

Also known as: DMPK A;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q09013-11)

Also known as: DMPK B;

The sequence of this isoform differs from the canonical sequence as follows:
     378-382: Missing.

Isoform 3 (identifier: Q09013-16)

Also known as: DMPK C;

The sequence of this isoform differs from the canonical sequence as follows:
     550-629: LDGPPAVAVG...WRRPGAARAP → MAPRPWLWAS...AQEPPALPEP

Note: No experimental confirmation available.

Isoform 4 (identifier: Q09013-15)

Also known as: DMPK D;

The sequence of this isoform differs from the canonical sequence as follows:
     378-382: Missing.
     550-629: LDGPPAVAVG...WRRPGAARAP → MAPRPWLWAS...AQEPPALPEP

Isoform 5 (identifier: Q09013-10)

Also known as: DMPK E;

The sequence of this isoform differs from the canonical sequence as follows:
     534-535: AV → GP
     536-629: Missing.

Note: No experimental confirmation available.

Isoform 6 (identifier: Q09013-12)

Also known as: DMPK F;

The sequence of this isoform differs from the canonical sequence as follows:
     378-382: Missing.
     534-535: AV → GP
     536-629: Missing.

Note: No experimental confirmation available.

Isoform 7 (identifier: Q09013-1)

The sequence of this isoform differs from the canonical sequence as follows:
     1-53: MSAEVRLRRL...DKYVADFLQW → MGGHFWPPEP...PRFFSPTTPP

Isoform 8 (identifier: Q09013-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-89: Missing.

Note: No experimental confirmation available.

Isoform 9 (identifier: Q09013-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-53: MSAEVRLRRL...DKYVADFLQW → MGGHFWPPEP...PRFFSPTTPP
     226-275: Missing.

Note: No experimental confirmation available.

Isoform 10 (identifier: Q09013-6)

The sequence of this isoform differs from the canonical sequence as follows:
     1-53: MSAEVRLRRL...DKYVADFLQW → MGGHFWPPEP...PRFFSPTTPP
     378-382: Missing.

Note: No experimental confirmation available.

Isoform 11 (identifier: Q09013-7)

The sequence of this isoform differs from the canonical sequence as follows:
     1-53: MSAEVRLRRL...DKYVADFLQW → MGGHFWPPEP...PRFFSPTTPP
     550-579: Missing.

Note: No experimental confirmation available.

Isoform 12 (identifier: Q09013-8)

The sequence of this isoform differs from the canonical sequence as follows:
     1-53: MSAEVRLRRL...DKYVADFLQW → MGGHFWPPEP...PRFFSPTTPP
     534-535: AV → GP
     536-629: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 629

629

Myotonin-protein kinase

PRO_0000085924

Regions

Topological domain

1 – 590

590

Cytoplasmic Potential

Transmembrane

591 – 611

21

Helical; Anchor for type IV membrane protein; Potential

Topological domain

612 – 629

18

Lumenal Potential

Domain

71 – 339

269

Protein kinase

Domain

340 – 415

76

AGC-kinase C-terminal

Nucleotide binding

77 – 85

9

ATP By similarity

Coiled coil

457 – 536

80

Ref.23 Ref.24

Sites

Active site

195

1

Proton acceptor By similarity

Binding site

100

1

ATP

Amino acid modifications

Modified residue

216

1

Phosphoserine; by autocatalysis By similarity

Modified residue

228

1

Phosphoserine; by autocatalysis By similarity

Modified residue

234

1

Phosphothreonine; by autocatalysis By similarity

Natural variations

Alternative sequence

1 – 89

89

Missing in isoform 8.

VSP_042098

Alternative sequence

1 – 53

53

MSAEV…DFLQW → MGGHFWPPEPYTVFMWGSPW EADSPRVKLRGREKGRQTEG GAFPLVSSALSGDPRFFSPT TPP in isoform 7, isoform 9, isoform 10, isoform 11 and isoform 12.

VSP_042099

Alternative sequence

226 – 275

50

Missing in isoform 9.

VSP_042100

Alternative sequence

378 – 382

5

Missing in isoform 2, isoform 4, isoform 6 and isoform 10.

VSP_042101

Alternative sequence

534 – 535

2

AV → GP in isoform 5, isoform 6 and isoform 12.

VSP_042102

Alternative sequence

536 – 629

94

Missing in isoform 5, isoform 6 and isoform 12.

VSP_042103

Alternative sequence

550 – 629

80

LDGPP…AARAP → MAPRPWLWASARWWGQAPCT AATCCSLPGSLGLAYRRRFP CSCSPLFCLVPPPWAALGWW PTPANSPQSGAAQEPPALPE P in isoform 3 and isoform 4.

VSP_042104

Alternative sequence

550 – 579

30

Missing in isoform 11.

VSP_042105

Natural variant

423

1

L → V. Ref.2 Ref.3 Ref.4 Ref.8
Corresponds to variant rs527221 [ dbSNP | Ensembl ].

VAR_058334

Natural variant

428

1

L → V in a lung small cell carcinoma sample; somatic mutation. Ref.26

VAR_040452

Experimental info

Mutagenesis

100

1

K → A: Loss of kinase activity. Ref.18

Sequence conflict

474

1

A → P in AAB31800. Ref.5

Secondary structure

1

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629

Helix Strand Turn

Details...

Helix

12 – 15

4

Turn

17 – 19

3

Helix

22 – 37

16

Helix

40 – 43

4

Helix

45 – 64

20

Helix

68 – 70

3

Beta strand

71 – 79

9

Beta strand

84 – 90

7

Turn

91 – 93

3

Beta strand

96 – 103

8

Helix

104 – 110

7

Helix

111 – 113

3

Helix

116 – 125

10

Turn

128 – 130

3

Beta strand

134 – 139

6

Beta strand

141 – 148

8

Helix

156 – 163

8

Helix

169 – 188

20

Helix

198 – 200

3

Beta strand

201 – 203

3

Beta strand

209 – 211

3

Helix

235 – 237

3

Helix

240 – 247

8

Beta strand

253 – 255

3

Helix

258 – 273

16

Helix

283 – 291

9

Helix

293 – 296

4

Helix

308 – 315

8

Helix

321 – 323

3

Turn

325 – 329

5

Helix

330 – 334

5

Helix

337 – 339

3

Beta strand

378 – 382

5

Turn

385 – 387

3

Helix

398 – 400

3

Helix

412 – 414

3

Helix

468 – 528

61

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (DMPK A) [UniParc]. Last modified December 14, 2011. Version 3. Checksum: 46783ED4AE65B493	FASTA	629	69,385
	10 20 30 40 50 60 MSAEVRLRRL QQLVLDPGFL GLEPLLDLLL GVHQELGASE LAQDKYVADF LQWAEPIVVR 70 80 90 100 110 120 LKEVRLQRDD FEILKVIGRG AFSEVAVVKM KQTGQVYAMK IMNKWDMLKR GEVSCFREER 130 140 150 160 170 180 DVLVNGDRRW ITQLHFAFQD ENYLYLVMEY YVGGDLLTLL SKFGERIPAE MARFYLAEIV 190 200 210 220 230 240 MAIDSVHRLG YVHRDIKPDN ILLDRCGHIR LADFGSCLKL RADGTVRSLV AVGTPDYLSP 250 260 270 280 290 300 EILQAVGGGP GTGSYGPECD WWALGVFAYE MFYGQTPFYA DSTAETYGKI VHYKEHLSLP 310 320 330 340 350 360 LVDEGVPEEA RDFIQRLLCP PETRLGRGGA GDFRTHPFFF GLDWDGLRDS VPPFTPDFEG 370 380 390 400 410 420 ATDTCNFDLV EDGLTAMVSG GGETLSDIRE GAPLGVHLPF VGYSYSCMAL RDSEVPGPTP 430 440 450 460 470 480 MELEAEQLLE PHVQAPSLEP SVSPQDETAE VAVPAAVPAA EAEAEVTLRE LQEALEEEVL 490 500 510 520 530 540 TRQSLSREME AIRTDNQNFA SQLREAEARN RDLEAHVRQL QERMELLQAE GATAVTGVPS 550 560 570 580 590 600 PRATDPPSHL DGPPAVAVGQ CPLVGPGPMH RRHLLLPARV PRPGLSEALS LLLFAVVLSR 610 620 AAALGCIGLV AHAGQLTAVW RRPGAARAP
	Isoform 2 (DMPK B) [UniParc]. Checksum: 7ECA31ED9A84E7E1	FASTA	624	69,028
	10 20 30 40 50 60 MSAEVRLRRL QQLVLDPGFL GLEPLLDLLL GVHQELGASE LAQDKYVADF LQWAEPIVVR 70 80 90 100 110 120 LKEVRLQRDD FEILKVIGRG AFSEVAVVKM KQTGQVYAMK IMNKWDMLKR GEVSCFREER 130 140 150 160 170 180 DVLVNGDRRW ITQLHFAFQD ENYLYLVMEY YVGGDLLTLL SKFGERIPAE MARFYLAEIV 190 200 210 220 230 240 MAIDSVHRLG YVHRDIKPDN ILLDRCGHIR LADFGSCLKL RADGTVRSLV AVGTPDYLSP 250 260 270 280 290 300 EILQAVGGGP GTGSYGPECD WWALGVFAYE MFYGQTPFYA DSTAETYGKI VHYKEHLSLP 310 320 330 340 350 360 LVDEGVPEEA RDFIQRLLCP PETRLGRGGA GDFRTHPFFF GLDWDGLRDS VPPFTPDFEG 370 380 390 400 410 420 ATDTCNFDLV EDGLTAMETL SDIREGAPLG VHLPFVGYSY SCMALRDSEV PGPTPMELEA 430 440 450 460 470 480 EQLLEPHVQA PSLEPSVSPQ DETAEVAVPA AVPAAEAEAE VTLRELQEAL EEEVLTRQSL 490 500 510 520 530 540 SREMEAIRTD NQNFASQLRE AEARNRDLEA HVRQLQERME LLQAEGATAV TGVPSPRATD 550 560 570 580 590 600 PPSHLDGPPA VAVGQCPLVG PGPMHRRHLL LPARVPRPGL SEALSLLLFA VVLSRAAALG 610 620 CIGLVAHAGQ LTAVWRRPGA ARAP
	Isoform 3 (DMPK C) [UniParc]. Checksum: 52B2B388CD99AA2F	FASTA	630	69,950
	10 20 30 40 50 60 MSAEVRLRRL QQLVLDPGFL GLEPLLDLLL GVHQELGASE LAQDKYVADF LQWAEPIVVR 70 80 90 100 110 120 LKEVRLQRDD FEILKVIGRG AFSEVAVVKM KQTGQVYAMK IMNKWDMLKR GEVSCFREER 130 140 150 160 170 180 DVLVNGDRRW ITQLHFAFQD ENYLYLVMEY YVGGDLLTLL SKFGERIPAE MARFYLAEIV 190 200 210 220 230 240 MAIDSVHRLG YVHRDIKPDN ILLDRCGHIR LADFGSCLKL RADGTVRSLV AVGTPDYLSP 250 260 270 280 290 300 EILQAVGGGP GTGSYGPECD WWALGVFAYE MFYGQTPFYA DSTAETYGKI VHYKEHLSLP 310 320 330 340 350 360 LVDEGVPEEA RDFIQRLLCP PETRLGRGGA GDFRTHPFFF GLDWDGLRDS VPPFTPDFEG 370 380 390 400 410 420 ATDTCNFDLV EDGLTAMVSG GGETLSDIRE GAPLGVHLPF VGYSYSCMAL RDSEVPGPTP 430 440 450 460 470 480 MELEAEQLLE PHVQAPSLEP SVSPQDETAE VAVPAAVPAA EAEAEVTLRE LQEALEEEVL 490 500 510 520 530 540 TRQSLSREME AIRTDNQNFA SQLREAEARN RDLEAHVRQL QERMELLQAE GATAVTGVPS 550 560 570 580 590 600 PRATDPPSHM APRPWLWASA RWWGQAPCTA ATCCSLPGSL GLAYRRRFPC SCSPLFCLVP 610 620 630 PPWAALGWWP TPANSPQSGA AQEPPALPEP
	Isoform 4 (DMPK D) [UniParc]. Checksum: 10EA0187F4AD4B7C	FASTA	625	69,592
	10 20 30 40 50 60 MSAEVRLRRL QQLVLDPGFL GLEPLLDLLL GVHQELGASE LAQDKYVADF LQWAEPIVVR 70 80 90 100 110 120 LKEVRLQRDD FEILKVIGRG AFSEVAVVKM KQTGQVYAMK IMNKWDMLKR GEVSCFREER 130 140 150 160 170 180 DVLVNGDRRW ITQLHFAFQD ENYLYLVMEY YVGGDLLTLL SKFGERIPAE MARFYLAEIV 190 200 210 220 230 240 MAIDSVHRLG YVHRDIKPDN ILLDRCGHIR LADFGSCLKL RADGTVRSLV AVGTPDYLSP 250 260 270 280 290 300 EILQAVGGGP GTGSYGPECD WWALGVFAYE MFYGQTPFYA DSTAETYGKI VHYKEHLSLP 310 320 330 340 350 360 LVDEGVPEEA RDFIQRLLCP PETRLGRGGA GDFRTHPFFF GLDWDGLRDS VPPFTPDFEG 370 380 390 400 410 420 ATDTCNFDLV EDGLTAMETL SDIREGAPLG VHLPFVGYSY SCMALRDSEV PGPTPMELEA 430 440 450 460 470 480 EQLLEPHVQA PSLEPSVSPQ DETAEVAVPA AVPAAEAEAE VTLRELQEAL EEEVLTRQSL 490 500 510 520 530 540 SREMEAIRTD NQNFASQLRE AEARNRDLEA HVRQLQERME LLQAEGATAV TGVPSPRATD 550 560 570 580 590 600 PPSHMAPRPW LWASARWWGQ APCTAATCCS LPGSLGLAYR RRFPCSCSPL FCLVPPPWAA 610 620 LGWWPTPANS PQSGAAQEPP ALPEP
	Isoform 5 (DMPK E) [UniParc]. Checksum: 9A08CEA02FAE8828	FASTA	535	59,804
	10 20 30 40 50 60 MSAEVRLRRL QQLVLDPGFL GLEPLLDLLL GVHQELGASE LAQDKYVADF LQWAEPIVVR 70 80 90 100 110 120 LKEVRLQRDD FEILKVIGRG AFSEVAVVKM KQTGQVYAMK IMNKWDMLKR GEVSCFREER 130 140 150 160 170 180 DVLVNGDRRW ITQLHFAFQD ENYLYLVMEY YVGGDLLTLL SKFGERIPAE MARFYLAEIV 190 200 210 220 230 240 MAIDSVHRLG YVHRDIKPDN ILLDRCGHIR LADFGSCLKL RADGTVRSLV AVGTPDYLSP 250 260 270 280 290 300 EILQAVGGGP GTGSYGPECD WWALGVFAYE MFYGQTPFYA DSTAETYGKI VHYKEHLSLP 310 320 330 340 350 360 LVDEGVPEEA RDFIQRLLCP PETRLGRGGA GDFRTHPFFF GLDWDGLRDS VPPFTPDFEG 370 380 390 400 410 420 ATDTCNFDLV EDGLTAMVSG GGETLSDIRE GAPLGVHLPF VGYSYSCMAL RDSEVPGPTP 430 440 450 460 470 480 MELEAEQLLE PHVQAPSLEP SVSPQDETAE VAVPAAVPAA EAEAEVTLRE LQEALEEEVL 490 500 510 520 530 TRQSLSREME AIRTDNQNFA SQLREAEARN RDLEAHVRQL QERMELLQAE GATGP
	Isoform 6 (DMPK F) [UniParc]. Checksum: 5E41498FDA6C22D4	FASTA	530	59,446
	10 20 30 40 50 60 MSAEVRLRRL QQLVLDPGFL GLEPLLDLLL GVHQELGASE LAQDKYVADF LQWAEPIVVR 70 80 90 100 110 120 LKEVRLQRDD FEILKVIGRG AFSEVAVVKM KQTGQVYAMK IMNKWDMLKR GEVSCFREER 130 140 150 160 170 180 DVLVNGDRRW ITQLHFAFQD ENYLYLVMEY YVGGDLLTLL SKFGERIPAE MARFYLAEIV 190 200 210 220 230 240 MAIDSVHRLG YVHRDIKPDN ILLDRCGHIR LADFGSCLKL RADGTVRSLV AVGTPDYLSP 250 260 270 280 290 300 EILQAVGGGP GTGSYGPECD WWALGVFAYE MFYGQTPFYA DSTAETYGKI VHYKEHLSLP 310 320 330 340 350 360 LVDEGVPEEA RDFIQRLLCP PETRLGRGGA GDFRTHPFFF GLDWDGLRDS VPPFTPDFEG 370 380 390 400 410 420 ATDTCNFDLV EDGLTAMETL SDIREGAPLG VHLPFVGYSY SCMALRDSEV PGPTPMELEA 430 440 450 460 470 480 EQLLEPHVQA PSLEPSVSPQ DETAEVAVPA AVPAAEAEAE VTLRELQEAL EEEVLTRQSL 490 500 510 520 530 SREMEAIRTD NQNFASQLRE AEARNRDLEA HVRQLQERME LLQAEGATGP
	Isoform 7 [UniParc]. Checksum: 69A831604F7F8D38	FASTA	639	70,371
	10 20 30 40 50 60 MGGHFWPPEP YTVFMWGSPW EADSPRVKLR GREKGRQTEG GAFPLVSSAL SGDPRFFSPT 70 80 90 100 110 120 TPPAEPIVVR LKEVRLQRDD FEILKVIGRG AFSEVAVVKM KQTGQVYAMK IMNKWDMLKR 130 140 150 160 170 180 GEVSCFREER DVLVNGDRRW ITQLHFAFQD ENYLYLVMEY YVGGDLLTLL SKFGERIPAE 190 200 210 220 230 240 MARFYLAEIV MAIDSVHRLG YVHRDIKPDN ILLDRCGHIR LADFGSCLKL RADGTVRSLV 250 260 270 280 290 300 AVGTPDYLSP EILQAVGGGP GTGSYGPECD WWALGVFAYE MFYGQTPFYA DSTAETYGKI 310 320 330 340 350 360 VHYKEHLSLP LVDEGVPEEA RDFIQRLLCP PETRLGRGGA GDFRTHPFFF GLDWDGLRDS 370 380 390 400 410 420 VPPFTPDFEG ATDTCNFDLV EDGLTAMVSG GGETLSDIRE GAPLGVHLPF VGYSYSCMAL 430 440 450 460 470 480 RDSEVPGPTP MELEAEQLLE PHVQAPSLEP SVSPQDETAE VAVPAAVPAA EAEAEVTLRE 490 500 510 520 530 540 LQEALEEEVL TRQSLSREME AIRTDNQNFA SQLREAEARN RDLEAHVRQL QERMELLQAE 550 560 570 580 590 600 GATAVTGVPS PRATDPPSHL DGPPAVAVGQ CPLVGPGPMH RRHLLLPARV PRPGLSEALS 610 620 630 LLLFAVVLSR AAALGCIGLV AHAGQLTAVW RRPGAARAP
	Isoform 8 [UniParc]. Checksum: A7BB715CB845055C	FASTA	540	59,334
	10 20 30 40 50 60 MKQTGQVYAM KIMNKWDMLK RGEVSCFREE RDVLVNGDRR WITQLHFAFQ DENYLYLVME 70 80 90 100 110 120 YYVGGDLLTL LSKFGERIPA EMARFYLAEI VMAIDSVHRL GYVHRDIKPD NILLDRCGHI 130 140 150 160 170 180 RLADFGSCLK LRADGTVRSL VAVGTPDYLS PEILQAVGGG PGTGSYGPEC DWWALGVFAY 190 200 210 220 230 240 EMFYGQTPFY ADSTAETYGK IVHYKEHLSL PLVDEGVPEE ARDFIQRLLC PPETRLGRGG 250 260 270 280 290 300 AGDFRTHPFF FGLDWDGLRD SVPPFTPDFE GATDTCNFDL VEDGLTAMVS GGGETLSDIR 310 320 330 340 350 360 EGAPLGVHLP FVGYSYSCMA LRDSEVPGPT PMELEAEQLL EPHVQAPSLE PSVSPQDETA 370 380 390 400 410 420 EVAVPAAVPA AEAEAEVTLR ELQEALEEEV LTRQSLSREM EAIRTDNQNF ASQLREAEAR 430 440 450 460 470 480 NRDLEAHVRQ LQERMELLQA EGATAVTGVP SPRATDPPSH LDGPPAVAVG QCPLVGPGPM 490 500 510 520 530 540 HRRHLLLPAR VPRPGLSEAL SLLLFAVVLS RAAALGCIGL VAHAGQLTAV WRRPGAARAP
	Isoform 9 [UniParc]. Checksum: 2558F658CFA1FCE1	FASTA	589	65,076
	10 20 30 40 50 60 MGGHFWPPEP YTVFMWGSPW EADSPRVKLR GREKGRQTEG GAFPLVSSAL SGDPRFFSPT 70 80 90 100 110 120 TPPAEPIVVR LKEVRLQRDD FEILKVIGRG AFSEVAVVKM KQTGQVYAMK IMNKWDMLKR 130 140 150 160 170 180 GEVSCFREER DVLVNGDRRW ITQLHFAFQD ENYLYLVMEY YVGGDLLTLL SKFGERIPAE 190 200 210 220 230 240 MARFYLAEIV MAIDSVHRLG YVHRDIKPDN ILLDRCGHIR LADFGSCLKL RADGTTPFYA 250 260 270 280 290 300 DSTAETYGKI VHYKEHLSLP LVDEGVPEEA RDFIQRLLCP PETRLGRGGA GDFRTHPFFF 310 320 330 340 350 360 GLDWDGLRDS VPPFTPDFEG ATDTCNFDLV EDGLTAMVSG GGETLSDIRE GAPLGVHLPF 370 380 390 400 410 420 VGYSYSCMAL RDSEVPGPTP MELEAEQLLE PHVQAPSLEP SVSPQDETAE VAVPAAVPAA 430 440 450 460 470 480 EAEAEVTLRE LQEALEEEVL TRQSLSREME AIRTDNQNFA SQLREAEARN RDLEAHVRQL 490 500 510 520 530 540 QERMELLQAE GATAVTGVPS PRATDPPSHL DGPPAVAVGQ CPLVGPGPMH RRHLLLPARV 550 560 570 580 PRPGLSEALS LLLFAVVLSR AAALGCIGLV AHAGQLTAVW RRPGAARAP
	Isoform 10 [UniParc]. Checksum: 94F39ADE9A8F4AFC	FASTA	634	70,014
	10 20 30 40 50 60 MGGHFWPPEP YTVFMWGSPW EADSPRVKLR GREKGRQTEG GAFPLVSSAL SGDPRFFSPT 70 80 90 100 110 120 TPPAEPIVVR LKEVRLQRDD FEILKVIGRG AFSEVAVVKM KQTGQVYAMK IMNKWDMLKR 130 140 150 160 170 180 GEVSCFREER DVLVNGDRRW ITQLHFAFQD ENYLYLVMEY YVGGDLLTLL SKFGERIPAE 190 200 210 220 230 240 MARFYLAEIV MAIDSVHRLG YVHRDIKPDN ILLDRCGHIR LADFGSCLKL RADGTVRSLV 250 260 270 280 290 300 AVGTPDYLSP EILQAVGGGP GTGSYGPECD WWALGVFAYE MFYGQTPFYA DSTAETYGKI 310 320 330 340 350 360 VHYKEHLSLP LVDEGVPEEA RDFIQRLLCP PETRLGRGGA GDFRTHPFFF GLDWDGLRDS 370 380 390 400 410 420 VPPFTPDFEG ATDTCNFDLV EDGLTAMETL SDIREGAPLG VHLPFVGYSY SCMALRDSEV 430 440 450 460 470 480 PGPTPMELEA EQLLEPHVQA PSLEPSVSPQ DETAEVAVPA AVPAAEAEAE VTLRELQEAL 490 500 510 520 530 540 EEEVLTRQSL SREMEAIRTD NQNFASQLRE AEARNRDLEA HVRQLQERME LLQAEGATAV 550 560 570 580 590 600 TGVPSPRATD PPSHLDGPPA VAVGQCPLVG PGPMHRRHLL LPARVPRPGL SEALSLLLFA 610 620 630 VVLSRAAALG CIGLVAHAGQ LTAVWRRPGA ARAP
	Isoform 11 [UniParc]. Checksum: 58A97059F9590719	FASTA	609	67,263
	10 20 30 40 50 60 MGGHFWPPEP YTVFMWGSPW EADSPRVKLR GREKGRQTEG GAFPLVSSAL SGDPRFFSPT 70 80 90 100 110 120 TPPAEPIVVR LKEVRLQRDD FEILKVIGRG AFSEVAVVKM KQTGQVYAMK IMNKWDMLKR 130 140 150 160 170 180 GEVSCFREER DVLVNGDRRW ITQLHFAFQD ENYLYLVMEY YVGGDLLTLL SKFGERIPAE 190 200 210 220 230 240 MARFYLAEIV MAIDSVHRLG YVHRDIKPDN ILLDRCGHIR LADFGSCLKL RADGTVRSLV 250 260 270 280 290 300 AVGTPDYLSP EILQAVGGGP GTGSYGPECD WWALGVFAYE MFYGQTPFYA DSTAETYGKI 310 320 330 340 350 360 VHYKEHLSLP LVDEGVPEEA RDFIQRLLCP PETRLGRGGA GDFRTHPFFF GLDWDGLRDS 370 380 390 400 410 420 VPPFTPDFEG ATDTCNFDLV EDGLTAMVSG GGETLSDIRE GAPLGVHLPF VGYSYSCMAL 430 440 450 460 470 480 RDSEVPGPTP MELEAEQLLE PHVQAPSLEP SVSPQDETAE VAVPAAVPAA EAEAEVTLRE 490 500 510 520 530 540 LQEALEEEVL TRQSLSREME AIRTDNQNFA SQLREAEARN RDLEAHVRQL QERMELLQAE 550 560 570 580 590 600 GATAVTGVPS PRATDPPSHV PRPGLSEALS LLLFAVVLSR AAALGCIGLV AHAGQLTAVW RRPGAARAP
	Isoform 12 [UniParc]. Checksum: EF016FDBE3933553	FASTA	545	60,790
	10 20 30 40 50 60 MGGHFWPPEP YTVFMWGSPW EADSPRVKLR GREKGRQTEG GAFPLVSSAL SGDPRFFSPT 70 80 90 100 110 120 TPPAEPIVVR LKEVRLQRDD FEILKVIGRG AFSEVAVVKM KQTGQVYAMK IMNKWDMLKR 130 140 150 160 170 180 GEVSCFREER DVLVNGDRRW ITQLHFAFQD ENYLYLVMEY YVGGDLLTLL SKFGERIPAE 190 200 210 220 230 240 MARFYLAEIV MAIDSVHRLG YVHRDIKPDN ILLDRCGHIR LADFGSCLKL RADGTVRSLV 250 260 270 280 290 300 AVGTPDYLSP EILQAVGGGP GTGSYGPECD WWALGVFAYE MFYGQTPFYA DSTAETYGKI 310 320 330 340 350 360 VHYKEHLSLP LVDEGVPEEA RDFIQRLLCP PETRLGRGGA GDFRTHPFFF GLDWDGLRDS 370 380 390 400 410 420 VPPFTPDFEG ATDTCNFDLV EDGLTAMVSG GGETLSDIRE GAPLGVHLPF VGYSYSCMAL 430 440 450 460 470 480 RDSEVPGPTP MELEAEQLLE PHVQAPSLEP SVSPQDETAE VAVPAAVPAA EAEAEVTLRE 490 500 510 520 530 540 LQEALEEEVL TRQSLSREME AIRTDNQNFA SQLREAEARN RDLEAHVRQL QERMELLQAE GATGP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"An unstable triplet repeat in a gene related to myotonic muscular dystrophy." Fu Y.-H., Pizzuti A., Fenwick R.G. Jr., King J., Rajnarayan S., Dunne P.W., Dubel J., Nasser G.A., Ashizawa T., de Jong P.J., Wieringa B., Korneluk R., Perryman M.B., Epstein H.F., Caskey C.T. Science 255:1256-1258(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 7), INVOLVEMENT IN DM1.
[2]	"Genomic organization and transcriptional units at the myotonic dystrophy locus." Shaw D.J., McCurrach M., Rundle S.A., Harley H.G., Crow S.R., Sohn R., Thirion J.-P., Hamshere M.G., Buckler A.J., Harper P.S., Housman D.E., Brook J.D. Genomics 18:673-679(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 2), VARIANT VAL-423. Tissue: Brain and Muscle.
[3]	"Structure and genomic sequence of the myotonic dystrophy (DM kinase) gene." Mahadevan M.S., Amemiya C., Jansen G., Sabourin L., Baird S., Neville C.E., Wormskamp N., Segers B., Batzer M., Lamerdin J., de Jong P.J., Wieringa B., Korneluk R.G. Hum. Mol. Genet. 2:299-304(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1; 2; 5; 6), VARIANT VAL-423.
[4]	"Decreased expression of myotonin-protein kinase messenger RNA and protein in adult form of myotonic dystrophy." Fu Y.-H., Friedman D.L., Richards S., Pearlman J.A., Gibbs R.A., Pizzuti A., Ashizawa T., Perryman M.B., Scarlato G., Fenwick R.G. Jr., Caskey C.T. Science 260:235-238(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 7; 8; 9; 10; 11 AND 12), VARIANT VAL-423.
[5]	"Expression of a novel human myotonin protein kinase (MtPK) cDNA clone which encodes a protein with a thymopoietin-like domain in COS cells." Sasagawa N., Sorimachi H., Maruyama K., Arahata K., Ishiura S., Suzuki K. FEBS Lett. 351:22-26(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4). Tissue: Muscle.
[6]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Prostate.
[8]	"Molecular basis of myotonic dystrophy: expansion of a trinucleotide (CTG) repeat at the 3' end of a transcript encoding a protein kinase family member." Brook J.D., McCurrach M., Harley H.G., Buckler A.J., Church D., Aburatani H., Hunter K., Stanton V.P., Thirion J.-P., Hudson T., Sohn R., Zemelman B., Snell R.G., Rundle S.A., Crow S., Davies J., Shelbourne P., Buxton J. , Jones C., Juvonen V., Johnson K., Harper P.S., Shaw D.J., Housman D.E. Cell 68:799-808(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 43-629 (ISOFORM 2), INVOLVEMENT IN DM1, VARIANT VAL-423.
[9]	"Different expression of the myotonin protein kinase gene in discrete areas of human brain." Gennarelli M., Lucarelli M., Zelano G., Pizzuti A., Novelli G., Dallapiccola B. Biochem. Biophys. Res. Commun. 216:489-494(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 550-619 (ISOFORM 1), TISSUE SPECIFICITY. Tissue: Brain.
[10]	"Characterization of the myotonic dystrophy region predicts multiple protein isoform-encoding mRNAs." Jansen G., Mahadevan M.S., Amemiya C., Wormskamp N., Segers B., Hendriks W., O'Hoy K., Baird S., Sabourin L., Lennon G., Jap P.L., Iles D., Coerwinkel M., Hofker M., Carrano A.V., de Jong P.J., Korneluk R.G., Wieringa B. Nat. Genet. 1:261-266(1992) [PubMed] [Europe PMC] [Abstract] Cited for: ALTERNATIVE SPLICING, INVOLVEMENT IN DM1. Tissue: Brain and Heart.
[11]	"MKBP, a novel member of the small heat shock protein family, binds and activates the myotonic dystrophy protein kinase." Suzuki A., Sugiyama Y., Hayashi Y., Nyu-i N., Yoshida M., Nonaka I., Ishiura S., Arahata K., Ohno S. J. Cell Biol. 140:1113-1124(1998) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HSPB2, ENZYME REGULATION. Tissue: Muscle.
[12]	"Myotonic dystrophy protein kinase domains mediate localization, oligomerization, novel catalytic activity, and autoinhibition." Bush E.W., Helmke S.M., Birnbaum R.A., Perryman M.B. Biochemistry 39:8480-8490(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, ENZYME REGULATION, HOMODIMERIZATION, SUBCELLULAR LOCATION, PROTEOLYTIC PROCESSING.
[13]	"Rac-1 and Raf-1 kinases, components of distinct signaling pathways, activate myotonic dystrophy protein kinase." Shimizu M., Wang W., Walch E.T., Dunne P.W., Epstein H.F. FEBS Lett. 475:273-277(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH RAC1, PHOSPHORYLATION BY RAF1, ENZYME REGULATION.
[14]	"Constitutive and regulated modes of splicing produce six major myotonic dystrophy protein kinase (DMPK) isoforms with distinct properties." Groenen P.J.T.A., Wansink D.G., Coerwinkel M., van den Broek W., Jansen G., Wieringa B. Hum. Mol. Genet. 9:605-616(2000) [PubMed] [Europe PMC] [Abstract] Cited for: ALTERNATIVE SPLICING (ISOFORMS 1; 2; 3; 4; 5 AND 6).
[15]	"Phospholemman is a substrate for myotonic dystrophy protein kinase." Mounsey J.P., John J.E. III, Helmke S.M., Bush E.W., Gilbert J., Roses A.D., Perryman M.B., Jones L.R., Moorman J.R. J. Biol. Chem. 275:23362-23367(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF FXYD1/PLM.
[16]	"Myotonic dystrophy protein kinase phosphorylates the myosin phosphatase targeting subunit and inhibits myosin phosphatase activity." Muranyi A., Zhang R., Liu F., Hirano K., Ito M., Epstein H.F., Hartshorne D.J. FEBS Lett. 493:80-84(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF PPP1R12A.
[17]	"Homodimerization through coiled-coil regions enhances activity of the myotonic dystrophy protein kinase." Zhang R., Epstein H.F. FEBS Lett. 546:281-287(2003) [PubMed] [Europe PMC] [Abstract] Cited for: HOMODIMERIZATION, ENZYME REGULATION.
[18]	"Myotonic dystrophy protein kinase phosphorylates phospholamban and regulates calcium uptake in cardiomyocyte sarcoplasmic reticulum." Kaliman P., Catalucci D., Lam J.T., Kondo R., Gutierrez J.C., Reddy S., Palacin M., Zorzano A., Chien K.R., Ruiz-Lozano P. J. Biol. Chem. 280:8016-8021(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF PLN, MUTAGENESIS OF LYS-100, INTERACTION WITH PLN.
[19]	"Divergent mitochondrial and endoplasmic reticulum association of DMPK splice isoforms depends on unique sequence arrangements in tail anchors." van Herpen R.E., Oude Ophuis R.J., Wijers M., Bennink M.B., van de Loo F.A., Fransen J., Wieringa B., Wansink D.G. Mol. Cell. Biol. 25:1402-1414(2005) [PubMed] [Europe PMC] [Abstract] Cited for: ALTERNATIVE SPLICING, SUBCELLULAR LOCATION.
[20]	"Highly unstable sequence interruptions of the CTG repeat in the myotonic dystrophy gene." Musova Z., Mazanec R., Krepelova A., Ehler E., Vales J., Jaklova R., Prochazka T., Koukal P., Marikova T., Kraus J., Havlovicova M., Sedlacek Z. Am. J. Med. Genet. A 149:1365-1374(2009) [PubMed] [Europe PMC] [Abstract] Cited for: INVOLVEMENT IN DM1.
[21]	"Chelerythrine perturbs lamellar actomyosin filaments by selective inhibition of myotonic dystrophy kinase-related Cdc42-binding kinase." Tan I., Lai J., Yong J., Li S.F., Leung T. FEBS Lett. 585:1260-1268(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF PPP1R12A.
[22]	"Myotonic dystrophy protein kinase is critical for nuclear envelope integrity." Harmon E.B., Harmon M.L., Larsen T.D., Yang J., Glasford J.W., Perryman M.B. J. Biol. Chem. 286:40296-40306(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN NUCLEAR ENVELOPE STABILITY, SUBCELLULAR LOCATION, INTERACTION WITH LMNA.
[23]	"Crystallization and preliminary X-ray analysis of the coiled-coil domain of dystrophia myotonica kinase." Garcia P., Marino M., Mayans O. Acta Crystallogr. D 60:2336-2339(2004) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 460-537, COILED-COIL DOMAIN.
[24]	"Molecular insights into the self-assembly mechanism of dystrophia myotonica kinase." Garcia P., Ucurum Z., Bucher R., Svergun D.I., Huber T., Lustig A., Konarev P.V., Marino M., Mayans O. FASEB J. 20:1142-1151(2006) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 460-537, SUBUNIT, COILED-COIL DOMAIN.
[25]	"Structure of dystrophia myotonica protein kinase." Elkins J.M., Amos A., Niesen F.H., Pike A.C.W., Fedorov O., Knapp S. Protein Sci. 18:782-791(2009) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 11-430 IN COMPLEX WITH INHIBITOR BIM-8, SUBUNIT.
[26]	"Patterns of somatic mutation in human cancer genomes." Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G. , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R. Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] VAL-428.
+	Additional computationally mapped references.

Web resources

GeneReviews

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M87312 mRNA. No translation available.
L19268 mRNA. Translation: AAA36206.1.
L19266 Genomic DNA. Translation: AAA36205.1.
L08835 Genomic DNA. Translation: AAC14449.1.
L08835 Genomic DNA. Translation: AAC14451.1.
L08835 Genomic DNA. Translation: AAC14448.1.
L08835 Genomic DNA. Translation: AAC14450.1.
L00727 Genomic DNA. Translation: AAA75235.1.
L00727 Genomic DNA. Translation: AAA75236.1.
L00727 Genomic DNA. Translation: AAA75237.1.
L00727 Genomic DNA. Translation: AAA75238.1.
L00727 Genomic DNA. Translation: AAA75239.1.
L00727 Genomic DNA. Translation: AAA75240.1.
S72883 mRNA. Translation: AAB31800.1.
CH471126 Genomic DNA. Translation: EAW57382.1.
BC062553 mRNA. Translation: AAH62553.1.
M94203 mRNA. Translation: AAA64884.1. Frameshift.
U46546 mRNA. Translation: AAA87583.1. Sequence problems.

IPI

IPI00215958.
IPI00215962.
IPI00220439.
IPI00220440.
IPI00220441.
IPI00220442.
IPI00220443.
IPI00305254.
IPI00418464.
IPI00555911.
IPI00790469.
IPI00855901.
IPI01011451.

PIR

B49364.

RefSeq

NP_001075029.1. NM_001081560.1.
NP_001075031.1. NM_001081562.1.
NP_001075032.1. NM_001081563.1.
NP_004400.4. NM_004409.3.

UniGene

Hs.631596.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1WT6	X-ray	1.60	A/B/D	460-537	[»]
2VD5	X-ray	2.80	A/B	11-420	[»]

ProteinModelPortal

Q09013.

SMR

Q09013. Positions 11-416, 461-527.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q09013. 9 interactions.

MINT

MINT-195910.

STRING

9606.ENSP00000345997.

PTM databases

PhosphoSite

Q09013.

Polymorphism databases

DMDM

254763287.

2D gel databases

REPRODUCTION-2DPAGE

Q09013.

Proteomic databases

PaxDb

Q09013.

PRIDE

Q09013.

Protocols and materials databases

DNASU

1760.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000291270; ENSP00000291270; ENSG00000104936.
ENST00000343373; ENSP00000345997; ENSG00000104936.
ENST00000354227; ENSP00000346168; ENSG00000104936.
ENST00000447742; ENSP00000413417; ENSG00000104936.
ENST00000458663; ENSP00000401753; ENSG00000104936.

GeneID

1760.

KEGG

hsa:1760.

UCSC

uc002pdd.1. human.
uc010xxt.1. human.

Organism-specific databases

CTD

1760.

GeneCards

GC19M046272.

H-InvDB

HIX0137522.

HGNC

HGNC:2933. DMPK.

HPA

HPA007164.
HPA008905.

MIM

160900. phenotype.
605377. gene.

neXtProt

NX_Q09013.

Orphanet

273. Steinert myotonic dystrophy.

PharmGKB

PA27380.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0515.

HOGENOM

HOG000233033.

HOVERGEN

HBG107817.

KO

K08788.

Enzyme and pathway databases

BRENDA

2.7.11.1. 2681.

Gene expression databases

ArrayExpress

Q09013.

Bgee

Q09013.

CleanEx

HS_DMPK.

Genevestigator

Q09013.

GermOnline

ENSG00000104936. Homo sapiens.

Family and domain databases

InterPro

IPR000961. AGC-kinase_C.
IPR011009. Kinase-like_dom.
IPR014930. Myotonic_dystrophy_kinase_coil.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]

Pfam

PF08826. DMPK_coil. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]

ProDom

PD011252. Myotonic_dystrophy_kinase_coil. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SMART

SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]

SUPFAM

SSF56112. Kinase_like. 1 hit.

PROSITE

PS51285. AGC_KINASE_CTER. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

Q09013.

ChEMBL

CHEMBL5320.

ChiTaRS

DMPK. human.

EvolutionaryTrace

Q09013.

GenomeRNAi

1760.

NextBio

7169.

SOURCE

Search...

Entry information

Entry name

DMPK_HUMAN

Accession

Primary (citable) accession number: Q09013
Secondary accession number(s): Q16205, Q6P5Z6

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	December 14, 2011
Last modified:	May 1, 2013
This is version 140 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.